Single active-site mutants are sufficient to enhance serine:pyruvate α-transaminase activity in an ω-transaminase
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چکیده
منابع مشابه
Transaminase activity in human blood.
Enzymatic transamination consists of the enzyme catalyzed reversible transfer of the alpha amino nitrogen of an amino acid to an alpha-keto acid with the synthesis of a second amino acid and a second alpha-keto acid. Enzymes catalyzing different transamination reactions are found widely distributed in animal tissues and have been shown to change in activity in some tissues during disease (1-3)....
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It is now believed that the amino groups of isoleucine and valine are accepted by their respective carbon chains during biosynthesis via a transamination. Most of the evidence for this hypothesis has been derived from experiments on isoleucineless and valineless mutants of Escherichia coli and Neurospora crassu (l-4). It is not positively established whether this transamination step can be medi...
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An efficient single-enzymatic cascade approach for the asymmetric synthesis of chiral amines has been developed, which applies the amino donor 3-aminocyclohexa-1,5-dienecarboxylic acid spontaneously tautomerizing to reach reaction completion with excellent ee values.
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Chiral amines are important for the chemical and pharmaceutical industries, and there is rapidly growing interest to use transaminases for their synthesis. Since the cost of the enzyme is an important factor for process economy, the use of whole-cell biocatalysts is attractive, since expensive purification and immobilization steps can be avoided. Display of the protein on the cell surface provi...
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THE quantitative and serial changes that occur in serum glutamic-oxaloacetic transaminase (SGOT) activity during the course of a myocardial infarction are well recognized. Changes in SGOT activity have been observed in other diseases such as hepatitis and pancreatitis (Wroblewski and LaDue, '955; Chinsky, Shmagranoff and Sherry, 1956) and after the administration of drugs such as chlorpromazine...
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ژورنال
عنوان ژورنال: FEBS Journal
سال: 2015
ISSN: 1742-464X
DOI: 10.1111/febs.13293